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P54741 (AFSK_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase AfsK

EC=2.7.11.1
Gene names
Name:afsK
Ordered Locus Names:SCO4423
ORF Names:SC6F11.21, SCD6.01
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]
Taxonomic identifier100226 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group

Protein attributes

Sequence length799 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the regulation of secondary metabolism by phosphorylating, on both Ser and Thr, the AfsR global regulatory protein involved in the control of secondary metabolism.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Interacts (via the N-terminal kinase domain) with KbpA; the interaction prevents autophosphorylation of AfsK. Ref.5

Post-translational modification

Autophosphorylated mainly on threonine residues. Some phosphorylation on serine residues. Autophosphorylation on Thr-168 is the major site enhancing kinase activity towards AfsR, and is regulated though interaction with KbpA. Ref.5 Ref.6

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 1 protein kinase domain.

Mass spectrometry

Molecular mass is 1638.8 Da from positions 68 - 93. Determined by ESI. Ref.6

Molecular mass is 1718.8 Da from positions 68 - 93. Determined by ESI. Monophosphorylated. Ref.6

Molecular mass is 2236.5 Da from positions 117 - 137. Determined by ESI. Ref.6

Molecular mass is 2109.4 Da from positions 167 - 186. Determined by ESI. Ref.6

Molecular mass is 2189.4 Da from positions 167 - 186. Determined by ESI. Monophosphorylated. Ref.6

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 799799Serine/threonine-protein kinase AfsK
PRO_0000171234

Regions

Domain16 – 271256Protein kinase
Nucleotide binding22 – 309ATP By similarity
Compositional bias317 – 428112Pro-rich

Sites

Active site1381Proton acceptor By similarity
Binding site441ATP By similarity

Amino acid modifications

Modified residue711Phosphoserine; by autocatalysis Ref.6
Modified residue1681Phosphothreonine; by autocatalysis Ref.6

Experimental info

Mutagenesis441K → A: No autophosphorylation. Binds KbpA. Ref.5
Mutagenesis711S → A: No autophosphorylation. Ref.6
Mutagenesis1281S → A: No change in autophosphorylation. Ref.6
Mutagenesis1681T → A: Almost completely abolishes autophosphorylation. No enhancement of kinase activity on AfsR. Very little constitutive kinase activity. Ref.6
Mutagenesis1681T → D: Almost completely abolishes autophosphorylation. No enhancement of kinase activity on AfsR. Constitutive kinase activity. Ref.6
Mutagenesis1681T → E: Almost completely abolishes autophosphorylation. No enhancement of kinase activity on AfsR. Some constitutive kinase activity. Ref.6
Mutagenesis1701T → D: No change in autophosphorylation. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P54741 [UniParc].

Last modified August 14, 2001. Version 2.
Checksum: 4BE9BED4169F6F5B

FASTA79983,788
        10         20         30         40         50         60 
MVDQLTQHDP RRIGPFEVLG RLGAGGMGLV YLARSASGRR VAIKTVRTEL AEDQLFRVRF 

        70         80         90        100        110        120 
TREVEAARAV SGFYTAAVVD ADPRAAVPWL ATAYVPAPSL EEIVNECGPM PAQAVRWLAA 

       130        140        150        160        170        180 
GVAEALQSIH GAGLVHRDLK PSNVLVVEDG PRVIDFGIAS GVSNTRLTMT NVAVGTPAYM 

       190        200        210        220        230        240 
SPEQAKDSRS VTGASDVFSL GSMLVFAATG HPPFHGANPV ETVFMLLREG PDLEGLPDEL 

       250        260        270        280        290        300 
RPLIESCMQM EATGRPNPAD LQAQLAPHLF GSGSDDSGTA SAWLPERAVG LIEGRRNGRP 

       310        320        330        340        350        360 
AVKPATTAGG RGHGHGPSGA RAPVHAPPLP PPPAHDPVVP APPAHVPAVP APVGAPDGGP 

       370        380        390        400        410        420 
VRLPGAAVPI GPGPRVADMR AAAVAAPPPE SALAASWSRP RPGVNGADPA VPAPAPAPPE 

       430        440        450        460        470        480 
ASPAGWRPWR FRMSNDVWGT PRVAEDLVYV TSFEVHALDV ATGRRRFKTR DVAWSMAVAD 

       490        500        510        520        530        540 
GRIHASDGPT LFALDAREGA DLWRVQTDAW VYSLQADRGT VLTATRGGGV QAWEASAGQK 

       550        560        570        580        590        600 
LWEVTGAQTD FESPEAGAAL HDGTAYVWQD ARLRALDART GDERWSYPIG DAASCGGVPV 

       610        620        630        640        650        660 
RLTQAPDGYV YVAAGTRVLA LEVASGHVRW HFEAPAVFLA PPTFVPGPAV TGGGVYLADY 

       670        680        690        700        710        720 
LGTVYALDAT DGRDRWRIAT EARSSTDPVL VAAGHVHVGS GKGLYTLDAV TGTPKWRFQA 

       730        740        750        760        770        780 
GGDIVGAPAV AEGRIHFGSS DHLLYTLKAD DGRLRWKLAT GGEITGSPVV RDGIVYACSK 

       790 
DRCVYALDAE KGTGTARTT 

« Hide

References

« Hide 'large scale' references
[1]"Phosphorylation of the AfsR protein involved in secondary metabolism in Streptomyces species by a eukaryotic-type protein kinase."
Matsumoto A., Hong S.K., Ishizuka H., Horinouchi S., Beppu T.
Gene 146:47-56(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: A3(2) / NRRL B-16638.
[2]"The aerial mycelium-defective phenotype of Streptomyces griseus resulting from A-factor deficiency is suppressed by a Ser/Thr kinase of S. coelicolor A3(2)."
Ueda K., Umeyama T., Beppu T., Horinouchi S.
Gene 169:91-95(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: A3(2) / NRRL B-16638.
[3]Matsumoto A., Hong S., Ishizuka H., Horinouchi S., Beppu T., Umeyama T.
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 239-240.
[4]"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)."
Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. expand/collapse author list , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.
Nature 417:141-147(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-471 / A3(2) / M145.
[5]"Autophosphorylation of a bacterial serine/threonine kinase, AfsK, is inhibited by KbpA, an AfsK-binding protein."
Umeyama T., Horinouchi S.
J. Bacteriol. 183:5506-5512(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KBPA, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-44.
[6]"Self-activation of serine/threonine kinase AfsK on autophosphorylation at threonine-168."
Tomono A., Mashiko M., Shimazu T., Inoue H., Nagasawa H., Yoshida M., Ohnishi Y., Horinouchi S.
J. Antibiot. 59:117-123(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: AUTOPHOSPHORYLATION AT SER-71 AND THR-168, MASS SPECTROMETRY, MUTAGENESIS OF SER-71; SER-128; THR-168 AND THR-170.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D45382 Genomic DNA. Translation: BAA08229.2.
AL939120 Genomic DNA. Translation: CAD55483.1.
RefSeqNP_733637.1. NC_003888.3.

3D structure databases

ProteinModelPortalP54741.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING100226.SCO4423.

PTM databases

PhosSiteP1007968.

Proteomic databases

PRIDEP54741.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD55483; CAD55483; CAD55483.
GeneID1099863.
KEGGsco:SCO4423.
PATRIC23738656. VBIStrCoe124346_4492.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000033839.
OMARFRMSND.
OrthoDBEOG6Z0Q5X.

Enzyme and pathway databases

BRENDA2.7.11.1. 5998.

Family and domain databases

Gene3D2.140.10.10. 1 hit.
InterProIPR011009. Kinase-like_dom.
IPR018391. PQQ_beta_propeller_repeat.
IPR002372. PQQ_repeat.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR027295. Quinonprotein_ADH-like_fam.
IPR011047. Quinonprotein_ADH-like_supfam.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
PF01011. PQQ. 3 hits.
[Graphical view]
SMARTSM00564. PQQ. 9 hits.
[Graphical view]
SUPFAMSSF50998. SSF50998. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAFSK_STRCO
AccessionPrimary (citable) accession number: P54741
Secondary accession number(s): Q9F365, Q9L002
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: August 14, 2001
Last modified: May 14, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families